Solution structure of the cold-shock-like protein fromRickettsia rickettsii

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Abstract
Rocky Mountain spotted fever is caused byRickettsia rickettsiiinfection.R. rickettsiican be transmitted to mammals, including humans, through the bite of an infected hard-bodied tick of the family Ixodidae. Since theR. rickettsiigenome contains only one cold-shock-like protein and given the essential nature of cold-shock proteins in other bacteria, the structure of the cold-shock-like protein fromR. rickettsiiwas investigated. With the exception of a short α-helix found between β-strands 3 and 4, the solution structure of theR. rickettsiicold-shock-like protein has the typical Greek-key five-stranded β-barrel structure found in most cold-shock domains. Additionally, theR. rickettsiicold-shock-like protein, with a ΔGof unfolding of 18.4 kJ mol−1, has a similar stability when compared with other bacterial cold-shock proteins.

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